Hid1 (high-temperature-induced dauer-formation protein 1) family protein similar to Schizosaccharomyces pombe Hid-1 family protein P19A11.07c and Ubp5-interacting protein ftp105
High-temperature-induced dauer-formation protein; Hid1 (high-temperature-induced dauer-formation protein 1) represents proteins of approximately 800 residues long and is conserved from fungi to humans. Functionally it might be involved in vesicle secretion or be an inter-cellular signalling protein or be a novel insulin receptor. It was previously thought to contain up to seven potential transmembrane domains separated by regions of low complexity. However, biochemical membrane fraction analysis demonstrate that HID-1 is a peripheral membrane protein tightly associated with the Golgi apparatus but not a transmembrane protein predicted by the bioinformatic programs. Furthermore, it contains a conserved N-terminal myristoylation site was required for HID-1 binding to the Golgi apparatus.
The actual alignment was detected with superfamily member pfam12722:
Pssm-ID: 463680 [Multi-domain] Cd Length: 804 Bit Score: 120.59 E-value: 4.33e-28
High-temperature-induced dauer-formation protein; Hid1 (high-temperature-induced dauer-formation protein 1) represents proteins of approximately 800 residues long and is conserved from fungi to humans. Functionally it might be involved in vesicle secretion or be an inter-cellular signalling protein or be a novel insulin receptor. It was previously thought to contain up to seven potential transmembrane domains separated by regions of low complexity. However, biochemical membrane fraction analysis demonstrate that HID-1 is a peripheral membrane protein tightly associated with the Golgi apparatus but not a transmembrane protein predicted by the bioinformatic programs. Furthermore, it contains a conserved N-terminal myristoylation site was required for HID-1 binding to the Golgi apparatus.
Pssm-ID: 463680 [Multi-domain] Cd Length: 804 Bit Score: 120.59 E-value: 4.33e-28
High-temperature-induced dauer-formation protein; Hid1 (high-temperature-induced dauer-formation protein 1) represents proteins of approximately 800 residues long and is conserved from fungi to humans. Functionally it might be involved in vesicle secretion or be an inter-cellular signalling protein or be a novel insulin receptor. It was previously thought to contain up to seven potential transmembrane domains separated by regions of low complexity. However, biochemical membrane fraction analysis demonstrate that HID-1 is a peripheral membrane protein tightly associated with the Golgi apparatus but not a transmembrane protein predicted by the bioinformatic programs. Furthermore, it contains a conserved N-terminal myristoylation site was required for HID-1 binding to the Golgi apparatus.
Pssm-ID: 463680 [Multi-domain] Cd Length: 804 Bit Score: 120.59 E-value: 4.33e-28
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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